FMO DATABASE

FMODB ID: NNQRQ

Calculation Name: 4JG2-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4JG2

Chain ID: A

ChEMBL ID:

UniProt ID: Q73EI2

Base Structure: X-ray

Registration Date: 2023-09-23

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	185
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1814801.334389
FMO2-HF: Nuclear repulsion	1744860.447583
FMO2-HF: Total energy	-69940.886806
FMO2-MP2: Total energy	-70148.124635

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:-11:LYS)

Summations of interaction energy for fragment #1(A:-11:LYS)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-106.366	-102.921	53.555	-27.945	-29.058	-0.226

Interaction energy analysis for fragmet #1(A:-11:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.861 / q_NPA : 0.908

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	-9	THR	0	0.001	-0.006	3.878	3.772	6.125	-0.015	-1.201	-1.138	0.004
4	A	-8	GLU	-1	-0.771	-0.821	1.642	-143.703	-147.161	28.107	-13.707	-10.942	-0.148
5	A	-7	ASN	0	0.038	0.014	4.427	3.815	3.957	-0.001	-0.017	-0.124	0.000
6	A	-6	LEU	0	0.058	0.018	4.932	-1.993	-1.993	0.000	0.000	0.000	0.000
7	A	-5	TYR	0	-0.010	0.005	6.347	0.281	0.281	0.000	0.000	0.000	0.000
8	A	-4	PHE	0	-0.051	-0.033	7.209	1.516	1.516	0.000	0.000	0.000	0.000
9	A	-3	GLN	0	-0.066	-0.017	2.395	-5.695	-4.769	1.009	-0.705	-1.231	0.001
10	A	-2	SER	0	-0.012	-0.033	1.808	-19.893	-20.903	12.960	-6.159	-5.791	-0.062
11	A	-1	ASN	0	-0.011	-0.005	4.162	3.126	3.649	0.000	-0.180	-0.343	-0.001
12	A	0	ALA	0	0.012	0.014	4.892	5.403	5.403	0.000	0.000	0.000	0.000
13	A	4	GLN	0	0.029	0.005	2.252	-23.929	-20.365	9.231	-5.791	-7.004	-0.019
14	A	5	ASN	0	-0.017	-0.013	2.247	3.988	4.367	2.253	-0.349	-2.283	-0.001
15	A	6	ARG	1	0.873	0.922	3.525	24.243	24.269	0.011	0.164	-0.202	0.000
16	A	7	THR	0	0.029	0.010	6.932	1.773	1.773	0.000	0.000	0.000	0.000
17	A	8	LYS	1	0.916	0.970	5.469	40.513	40.513	0.000	0.000	0.000	0.000
18	A	9	VAL	0	0.006	0.007	6.903	-0.287	-0.287	0.000	0.000	0.000	0.000
19	A	10	VAL	0	-0.025	-0.021	7.961	-0.242	-0.242	0.000	0.000	0.000	0.000
20	A	11	THR	0	0.042	0.020	10.524	0.061	0.061	0.000	0.000	0.000	0.000
21	A	12	SER	0	0.034	0.000	13.928	-0.268	-0.268	0.000	0.000	0.000	0.000
22	A	13	VAL	0	0.003	-0.006	15.660	0.217	0.217	0.000	0.000	0.000	0.000
23	A	14	ASN	0	-0.003	0.010	18.122	0.907	0.907	0.000	0.000	0.000	0.000
24	A	15	THR	0	-0.007	0.012	17.623	0.351	0.351	0.000	0.000	0.000	0.000
25	A	16	ARG	1	0.850	0.928	20.213	10.419	10.419	0.000	0.000	0.000	0.000
26	A	17	LEU	0	-0.014	0.002	20.474	-0.362	-0.362	0.000	0.000	0.000	0.000
27	A	18	SER	0	0.096	0.036	23.960	0.674	0.674	0.000	0.000	0.000	0.000
28	A	19	TYR	0	-0.071	-0.048	25.937	-0.438	-0.438	0.000	0.000	0.000	0.000
29	A	20	PHE	0	-0.017	-0.011	22.132	-0.404	-0.404	0.000	0.000	0.000	0.000
30	A	21	HIS	0	0.022	0.016	24.645	0.473	0.473	0.000	0.000	0.000	0.000
31	A	22	GLY	0	0.044	0.013	22.094	-0.430	-0.430	0.000	0.000	0.000	0.000
32	A	23	TRP	0	0.000	-0.021	22.440	-0.582	-0.582	0.000	0.000	0.000	0.000
33	A	24	GLU	-1	-0.826	-0.890	25.036	-10.348	-10.348	0.000	0.000	0.000	0.000
34	A	25	PRO	0	-0.070	-0.016	24.762	-0.182	-0.182	0.000	0.000	0.000	0.000
35	A	26	VAL	0	0.084	0.033	26.229	0.355	0.355	0.000	0.000	0.000	0.000
36	A	27	SER	0	0.003	-0.001	27.953	-0.282	-0.282	0.000	0.000	0.000	0.000
37	A	28	ILE	0	-0.011	-0.014	26.682	0.046	0.046	0.000	0.000	0.000	0.000
38	A	29	ASN	0	-0.036	-0.027	30.651	-0.152	-0.152	0.000	0.000	0.000	0.000
39	A	30	GLY	0	0.086	0.058	33.625	0.140	0.140	0.000	0.000	0.000	0.000
40	A	31	GLY	0	-0.037	-0.008	29.946	-0.043	-0.043	0.000	0.000	0.000	0.000
41	A	32	ALA	0	-0.023	-0.022	27.179	-0.032	-0.032	0.000	0.000	0.000	0.000
42	A	33	GLU	-1	-0.897	-0.941	27.116	-10.795	-10.795	0.000	0.000	0.000	0.000
43	A	34	LYS	1	0.803	0.890	22.065	11.757	11.757	0.000	0.000	0.000	0.000
44	A	35	TYR	0	0.101	0.072	20.671	0.292	0.292	0.000	0.000	0.000	0.000
45	A	36	SER	0	-0.055	-0.055	21.476	-0.285	-0.285	0.000	0.000	0.000	0.000
46	A	37	VAL	0	0.030	0.009	20.399	0.146	0.146	0.000	0.000	0.000	0.000
47	A	38	SER	0	-0.038	-0.008	21.926	-0.368	-0.368	0.000	0.000	0.000	0.000
48	A	39	VAL	0	-0.021	-0.009	17.708	0.216	0.216	0.000	0.000	0.000	0.000
49	A	40	LEU	0	0.029	0.015	21.078	-0.040	-0.040	0.000	0.000	0.000	0.000
50	A	41	ILE	0	-0.012	-0.017	17.236	-0.410	-0.410	0.000	0.000	0.000	0.000
51	A	42	PRO	0	0.063	0.037	20.844	0.317	0.317	0.000	0.000	0.000	0.000
52	A	43	LYS	1	0.807	0.877	21.907	9.813	9.813	0.000	0.000	0.000	0.000
53	A	44	THR	0	-0.006	-0.008	22.995	-0.067	-0.067	0.000	0.000	0.000	0.000
54	A	45	ASP	-1	-0.777	-0.834	16.733	-15.778	-15.778	0.000	0.000	0.000	0.000
55	A	46	LYS	1	0.915	0.923	17.868	11.362	11.362	0.000	0.000	0.000	0.000
56	A	47	GLU	-1	-0.935	-0.944	12.205	-18.538	-18.538	0.000	0.000	0.000	0.000
57	A	48	THR	0	0.011	-0.021	13.379	-1.288	-1.288	0.000	0.000	0.000	0.000
58	A	49	ILE	0	-0.017	-0.008	14.324	-0.479	-0.479	0.000	0.000	0.000	0.000
59	A	50	ASN	0	-0.009	-0.003	14.717	0.368	0.368	0.000	0.000	0.000	0.000
60	A	51	ALA	0	0.007	0.015	10.112	-0.330	-0.330	0.000	0.000	0.000	0.000
61	A	52	ILE	0	0.015	0.003	11.705	-0.750	-0.750	0.000	0.000	0.000	0.000
62	A	53	ASN	0	-0.054	-0.034	13.836	0.351	0.351	0.000	0.000	0.000	0.000
63	A	54	ALA	0	0.011	0.009	11.725	0.172	0.172	0.000	0.000	0.000	0.000
64	A	55	ALA	0	0.026	0.021	10.315	-0.316	-0.316	0.000	0.000	0.000	0.000
65	A	56	VAL	0	-0.043	-0.026	11.808	0.061	0.061	0.000	0.000	0.000	0.000
66	A	57	ASP	-1	-0.830	-0.911	15.414	-14.222	-14.222	0.000	0.000	0.000	0.000
67	A	58	ALA	0	-0.021	-0.001	10.863	0.338	0.338	0.000	0.000	0.000	0.000
68	A	59	ALA	0	0.025	0.018	12.955	-0.017	-0.017	0.000	0.000	0.000	0.000
69	A	60	ILE	0	-0.054	-0.029	13.969	0.695	0.695	0.000	0.000	0.000	0.000
70	A	61	GLU	-1	-0.802	-0.872	14.869	-16.625	-16.625	0.000	0.000	0.000	0.000
71	A	62	GLU	-1	-0.855	-0.941	10.098	-25.381	-25.381	0.000	0.000	0.000	0.000
72	A	63	GLY	0	-0.005	0.001	14.497	0.222	0.222	0.000	0.000	0.000	0.000
73	A	64	ILE	0	-0.056	-0.031	17.630	0.522	0.522	0.000	0.000	0.000	0.000
74	A	65	ALA	0	-0.015	-0.008	15.586	0.497	0.497	0.000	0.000	0.000	0.000
75	A	66	LYS	1	0.906	0.976	16.211	16.125	16.125	0.000	0.000	0.000	0.000
76	A	67	PHE	0	-0.046	-0.039	17.979	0.335	0.335	0.000	0.000	0.000	0.000
77	A	68	GLY	0	0.038	0.042	21.415	0.649	0.649	0.000	0.000	0.000	0.000
78	A	69	GLY	0	-0.001	-0.005	23.372	-0.021	-0.021	0.000	0.000	0.000	0.000
79	A	70	LYS	1	0.952	0.971	24.726	9.521	9.521	0.000	0.000	0.000	0.000
80	A	71	LYS	1	0.913	0.931	18.726	14.357	14.357	0.000	0.000	0.000	0.000
81	A	72	PRO	0	-0.021	-0.001	22.198	0.500	0.500	0.000	0.000	0.000	0.000
82	A	73	ASN	0	0.039	0.011	24.455	-0.455	-0.455	0.000	0.000	0.000	0.000
83	A	74	LYS	1	0.907	0.919	19.599	13.844	13.844	0.000	0.000	0.000	0.000
84	A	75	ALA	0	0.032	0.025	24.839	-0.085	-0.085	0.000	0.000	0.000	0.000
85	A	76	ALA	0	-0.042	-0.012	27.693	0.311	0.311	0.000	0.000	0.000	0.000
86	A	77	ILE	0	-0.073	-0.044	22.210	-0.009	-0.009	0.000	0.000	0.000	0.000
87	A	78	LYS	1	0.924	0.960	24.007	11.140	11.140	0.000	0.000	0.000	0.000
88	A	79	LEU	0	0.038	0.010	20.826	-0.566	-0.566	0.000	0.000	0.000	0.000
89	A	80	PRO	0	-0.008	0.003	17.610	0.505	0.505	0.000	0.000	0.000	0.000
90	A	81	LEU	0	-0.011	-0.003	18.584	0.069	0.069	0.000	0.000	0.000	0.000
91	A	82	ARG	1	0.760	0.860	20.874	11.706	11.706	0.000	0.000	0.000	0.000
92	A	83	ASP	-1	-0.781	-0.892	24.358	-10.513	-10.513	0.000	0.000	0.000	0.000
93	A	84	GLY	0	0.004	-0.011	26.741	0.255	0.255	0.000	0.000	0.000	0.000
94	A	85	ASP	-1	-0.758	-0.858	28.339	-9.315	-9.315	0.000	0.000	0.000	0.000
95	A	86	VAL	0	-0.023	-0.013	30.600	0.298	0.298	0.000	0.000	0.000	0.000
96	A	87	GLU	-1	-0.829	-0.874	27.633	-10.564	-10.564	0.000	0.000	0.000	0.000
97	A	88	ARG	1	0.835	0.915	29.125	9.870	9.870	0.000	0.000	0.000	0.000
98	A	89	ASP	-1	-0.791	-0.887	32.491	-8.180	-8.180	0.000	0.000	0.000	0.000
99	A	90	ASP	-1	-0.854	-0.907	31.881	-9.067	-9.067	0.000	0.000	0.000	0.000
100	A	91	GLU	-1	-0.852	-0.945	32.631	-8.491	-8.491	0.000	0.000	0.000	0.000
101	A	92	ALA	0	-0.081	-0.035	29.925	-0.134	-0.134	0.000	0.000	0.000	0.000
102	A	93	TYR	0	-0.065	-0.044	26.918	-0.562	-0.562	0.000	0.000	0.000	0.000
103	A	94	LYS	1	0.887	0.947	28.613	8.394	8.394	0.000	0.000	0.000	0.000
104	A	95	GLY	0	0.007	0.009	28.924	-0.147	-0.147	0.000	0.000	0.000	0.000
105	A	96	HIS	0	-0.091	-0.059	24.050	-0.681	-0.681	0.000	0.000	0.000	0.000
106	A	97	TYR	0	-0.003	0.003	21.575	0.186	0.186	0.000	0.000	0.000	0.000
107	A	98	PHE	0	-0.010	-0.013	21.879	-0.176	-0.176	0.000	0.000	0.000	0.000
108	A	99	VAL	0	0.019	0.012	17.194	-0.145	-0.145	0.000	0.000	0.000	0.000
109	A	100	ASN	0	-0.020	-0.003	20.568	0.152	0.152	0.000	0.000	0.000	0.000
110	A	101	ALA	0	0.028	0.027	17.529	-0.138	-0.138	0.000	0.000	0.000	0.000
111	A	102	ASN	0	-0.040	-0.037	18.688	0.767	0.767	0.000	0.000	0.000	0.000
112	A	103	SER	0	0.036	0.020	16.293	-0.694	-0.694	0.000	0.000	0.000	0.000
113	A	104	LYS	1	0.953	0.974	18.887	13.203	13.203	0.000	0.000	0.000	0.000
114	A	105	THR	0	0.002	0.019	16.824	0.434	0.434	0.000	0.000	0.000	0.000
115	A	106	PRO	0	0.021	0.019	18.687	-0.320	-0.320	0.000	0.000	0.000	0.000
116	A	107	PRO	0	-0.042	0.001	16.044	-0.977	-0.977	0.000	0.000	0.000	0.000
117	A	108	GLN	0	0.037	0.006	13.189	-0.620	-0.620	0.000	0.000	0.000	0.000
118	A	109	ILE	0	-0.013	0.009	16.461	-0.746	-0.746	0.000	0.000	0.000	0.000
119	A	110	VAL	0	0.000	0.000	15.535	0.355	0.355	0.000	0.000	0.000	0.000
120	A	111	ASP	-1	-0.694	-0.837	18.933	-14.228	-14.228	0.000	0.000	0.000	0.000
121	A	112	LYS	1	0.886	0.932	18.488	12.374	12.374	0.000	0.000	0.000	0.000
122	A	113	ALA	0	-0.050	-0.011	18.745	-0.320	-0.320	0.000	0.000	0.000	0.000
123	A	114	VAL	0	-0.042	-0.024	13.440	-0.574	-0.574	0.000	0.000	0.000	0.000
124	A	115	ARG	1	0.897	0.935	16.791	12.882	12.882	0.000	0.000	0.000	0.000
125	A	116	PRO	0	-0.001	-0.015	19.155	0.087	0.087	0.000	0.000	0.000	0.000
126	A	117	ILE	0	-0.027	0.000	20.932	0.541	0.541	0.000	0.000	0.000	0.000
127	A	118	LEU	0	-0.027	-0.019	23.700	-0.047	-0.047	0.000	0.000	0.000	0.000
128	A	119	ASP	-1	-0.801	-0.889	26.897	-9.641	-9.641	0.000	0.000	0.000	0.000
129	A	120	ARG	1	0.850	0.886	27.574	10.355	10.355	0.000	0.000	0.000	0.000
130	A	121	ASN	0	-0.047	-0.040	28.568	-0.056	-0.056	0.000	0.000	0.000	0.000
131	A	122	GLU	-1	-0.865	-0.908	25.933	-11.268	-11.268	0.000	0.000	0.000	0.000
132	A	123	VAL	0	-0.050	-0.032	22.559	-0.344	-0.344	0.000	0.000	0.000	0.000
133	A	124	TYR	0	0.012	-0.023	25.797	0.121	0.121	0.000	0.000	0.000	0.000
134	A	125	SER	0	0.022	0.003	27.035	-0.489	-0.489	0.000	0.000	0.000	0.000
135	A	126	GLY	0	0.067	0.047	27.406	0.433	0.433	0.000	0.000	0.000	0.000
136	A	127	CYS	0	-0.068	0.016	25.047	-0.182	-0.182	0.000	0.000	0.000	0.000
137	A	128	TYR	0	0.042	-0.006	23.034	-0.073	-0.073	0.000	0.000	0.000	0.000
138	A	129	ALA	0	0.049	0.008	19.883	-0.036	-0.036	0.000	0.000	0.000	0.000
139	A	130	ARG	1	0.829	0.923	10.920	20.726	20.726	0.000	0.000	0.000	0.000
140	A	131	VAL	0	0.048	0.016	15.293	0.009	0.009	0.000	0.000	0.000	0.000
141	A	132	SER	0	-0.025	-0.015	10.081	-2.021	-2.021	0.000	0.000	0.000	0.000
142	A	133	LEU	0	-0.027	-0.014	11.138	1.258	1.258	0.000	0.000	0.000	0.000
143	A	134	ASN	0	0.026	0.018	8.365	-4.787	-4.787	0.000	0.000	0.000	0.000
144	A	135	PHE	0	0.018	0.006	10.931	1.946	1.946	0.000	0.000	0.000	0.000
145	A	136	TYR	0	0.006	-0.009	12.114	-0.985	-0.985	0.000	0.000	0.000	0.000
146	A	137	ALA	0	0.044	0.024	14.681	1.017	1.017	0.000	0.000	0.000	0.000
147	A	138	PHE	0	-0.054	-0.025	17.834	-0.103	-0.103	0.000	0.000	0.000	0.000
148	A	139	ASN	0	0.011	-0.018	20.915	0.575	0.575	0.000	0.000	0.000	0.000
149	A	140	SER	0	0.013	0.022	24.686	-0.053	-0.053	0.000	0.000	0.000	0.000
150	A	141	ASN	0	0.031	0.005	26.786	0.307	0.307	0.000	0.000	0.000	0.000
151	A	142	GLY	0	0.058	0.041	29.834	0.112	0.112	0.000	0.000	0.000	0.000
152	A	143	ASN	0	-0.055	-0.017	26.652	0.004	0.004	0.000	0.000	0.000	0.000
153	A	144	LYS	1	0.996	0.998	24.803	10.012	10.012	0.000	0.000	0.000	0.000
154	A	145	GLY	0	0.010	0.013	22.480	0.354	0.354	0.000	0.000	0.000	0.000
155	A	146	VAL	0	-0.037	-0.009	16.418	-0.450	-0.450	0.000	0.000	0.000	0.000
156	A	147	ALA	0	-0.014	0.002	17.922	0.675	0.675	0.000	0.000	0.000	0.000
157	A	148	CYS	0	-0.019	-0.021	15.384	-0.883	-0.883	0.000	0.000	0.000	0.000
158	A	149	GLY	0	0.031	0.025	14.487	0.827	0.827	0.000	0.000	0.000	0.000
159	A	150	LEU	0	-0.023	-0.016	13.972	-1.183	-1.183	0.000	0.000	0.000	0.000
160	A	151	GLY	0	0.016	0.005	12.369	-0.460	-0.460	0.000	0.000	0.000	0.000
161	A	152	ASN	0	-0.033	-0.035	12.049	1.746	1.746	0.000	0.000	0.000	0.000
162	A	153	ILE	0	0.020	0.015	14.161	-0.397	-0.397	0.000	0.000	0.000	0.000
163	A	154	GLN	0	-0.046	-0.027	15.520	-0.391	-0.391	0.000	0.000	0.000	0.000
164	A	155	LYS	1	0.804	0.890	17.539	11.817	11.817	0.000	0.000	0.000	0.000
165	A	156	ILE	0	-0.095	-0.044	17.532	-0.213	-0.213	0.000	0.000	0.000	0.000
166	A	157	ARG	1	0.874	0.931	21.620	11.986	11.986	0.000	0.000	0.000	0.000
167	A	158	ASP	-1	-0.741	-0.844	25.285	-11.117	-11.117	0.000	0.000	0.000	0.000
168	A	159	GLY	0	-0.034	-0.027	28.374	-0.094	-0.094	0.000	0.000	0.000	0.000
169	A	160	GLU	-1	-0.892	-0.931	30.153	-8.700	-8.700	0.000	0.000	0.000	0.000
170	A	161	PRO	0	0.012	0.003	31.654	-0.296	-0.296	0.000	0.000	0.000	0.000
171	A	162	LEU	0	-0.043	-0.020	28.707	0.169	0.169	0.000	0.000	0.000	0.000
172	A	163	GLY	0	0.024	0.011	32.577	-0.058	-0.058	0.000	0.000	0.000	0.000
173	A	164	GLY	0	0.004	0.003	32.703	-0.330	-0.330	0.000	0.000	0.000	0.000
174	A	165	ARG	1	0.909	0.948	27.104	10.803	10.803	0.000	0.000	0.000	0.000
175	A	166	THR	0	0.012	0.007	34.414	-0.005	-0.005	0.000	0.000	0.000	0.000
176	A	167	ASN	0	-0.092	-0.068	35.194	0.144	0.144	0.000	0.000	0.000	0.000
177	A	168	ALA	0	0.058	0.040	37.341	0.011	0.011	0.000	0.000	0.000	0.000
178	A	169	ALA	0	-0.013	-0.008	40.309	0.134	0.134	0.000	0.000	0.000	0.000
179	A	170	ASP	-1	-0.900	-0.939	35.801	-8.580	-8.580	0.000	0.000	0.000	0.000
180	A	171	ASP	-1	-0.967	-0.970	38.484	-8.236	-8.236	0.000	0.000	0.000	0.000
181	A	172	PHE	0	-0.082	-0.043	40.782	0.170	0.170	0.000	0.000	0.000	0.000
182	A	173	THR	0	-0.009	-0.006	44.446	-0.059	-0.059	0.000	0.000	0.000	0.000
183	A	174	THR	0	-0.044	-0.053	46.953	-0.024	-0.024	0.000	0.000	0.000	0.000
184	A	175	ILE	0	-0.027	-0.007	50.008	-0.007	-0.007	0.000	0.000	0.000	0.000
185	A	176	GLU	-1	-0.912	-0.923	52.799	-5.889	-5.889	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-11:LYS)